MAGI3_CHICK
ID MAGI3_CHICK Reviewed; 1128 AA.
AC Q5F488;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3;
DE AltName: Full=Membrane-associated guanylate kinase inverted 3;
DE Short=MAGI-3;
GN Name=MAGI3; ORFNames=RCJMB04_2d13;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Acts as a scaffolding protein at cell-cell junctions, thereby
CC regulating various cellular and signaling processes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AJ851412; CAH65046.1; -; mRNA.
DR RefSeq; NP_001012715.1; NM_001012697.1.
DR AlphaFoldDB; Q5F488; -.
DR SMR; Q5F488; -.
DR STRING; 9031.ENSGALP00000002804; -.
DR PaxDb; Q5F488; -.
DR GeneID; 419877; -.
DR KEGG; gga:419877; -.
DR CTD; 260425; -.
DR VEuPathDB; HostDB:geneid_419877; -.
DR eggNOG; KOG0707; Eukaryota.
DR eggNOG; KOG3209; Eukaryota.
DR InParanoid; Q5F488; -.
DR OrthoDB; 284488at2759; -.
DR PhylomeDB; Q5F488; -.
DR PRO; PR:Q5F488; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0046328; P:regulation of JNK cascade; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.30.42.10; -; 6.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR030035; MAGI3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10316:SF10; PTHR10316:SF10; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 4.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 6.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF50156; SSF50156; 6.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell junction; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1128
FT /note="Membrane-associated guanylate kinase, WW and PDZ
FT domain-containing protein 3"
FT /id="PRO_0000341410"
FT DOMAIN 22..108
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 116..290
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 295..328
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 341..374
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 412..494
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 581..657
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 728..810
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 852..939
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1024..1106
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 184..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
SQ SEQUENCE 1128 AA; 122702 MW; 1FFC4AB86413D58F CRC64;
MSKTLRKKRH WLSKVQECVV SWGGPAGPDP ELLHGGAERG EFPYLAGRLP TGAEGAPGPA
LLSGKAPAPG DVLLEVNGTP VSGLTHRDTL AVIRHFREPV RLKTVRPGKV INKDLRHYLS
LQFQKGSIDH KLQQVIRDNL YLRTIPCTTR APRDGEVPGV DYNFIPVEQF KALEESGALL
ESGTYDGNFY GTPKPPAEPS PFQPDPVDQV LFDNDFDTES QRKRTTSVSK MQRMDSSLPE
DEEEEEKEAV NGSGGIENKE KHSDSSDWMK PVPSYNQTSS SMDFRNYMSR DETLEPLPKN
WEMAYTDTGM IYFIDHNTKT TTWLDPRLCK KAKAPEDCED GELPYGWEKI EDPQYGTYYV
DHINQKTQFE NPVLEAKRKK QLGQTDGGPS KSVPEKSLFT RDPSQLIGAL IRTSLKKSTM
GFGFTIIGGD RPDEFLQVKN VLKDGPAAQD GRIAPGDVIV DINGNCVLGH THADVVQMFQ
LVPVNQYVNM TLCRGYPLPD DNEDPVVDIV TATPIINGPP VTKGDICLTS QELIAGTVVL
DQNGKTGPML VNGRLNGPSM DTNEQRISVA SSGGSQPELV TIPLVKGPKG FGFAIADSPT
GQKVKMILDS QWCQGLQKGD VIKEICHQNV QSLTHLQVVE VLKQFPIGAE VPLLILRGGP
PSPTKTGKMK DKQESSGSLE ALSDAIPQPM PFPPTAVRSG SPKLDPSEVY LKSKTMYEDK
PPNTRDLDVF LRKQESGFGF RVLGGDGADQ PIYIGAIIPL GAAEKDGRLR AADELMCIDG
VPVKGKSHKQ VLDLMTSAAR NGQVLLTVRR KIFFGGEKQA EEDESQAVVT QNSSPRLNRA
EFATQQSPEV YDVCLQRKEN EGFGFVILTS KNKPPPGVIP HKIGRVIDGS PADQCGKLKV
GDRISAVNGQ SIVELSHDSI VQLIKDAGHV VTLTVVAEEE HRGPPSGTNS AKQSPAPQHR
PLGPAQSSAS STDRGATEGE AGKEVSNSYR LSWPEHKHLA QPDAGSASGV GSRHSQAQNS
GCFPVELERG PRGFGFSLRG GKEYNMGLFI LRLAEDGPAV KDGRVHVGDQ IVEINGEPTQ
GITHTRAIEL IQAGGNKVLL LLRPGTGLIP DHSLAPSSLC PYVKPEQH
